title: Development of a recombinant ε-poly-L-lysine synthetase expression system to perform mutational analysis.
abstract: ε-Poly-L-lysine (ε-PL) synthetase (Pls), which is a membrane protein with adenylation and thiolation domains characteristic of the nonribosomal peptide synthetases, catalyzes polymerization of L-lysine molecules (25-mer to 35-mer). Here, we report on the development of a recombinant Pls expression system that allowed us to perform a site-directed mutational analysis.
authors.affiliation: Yokohama Research Center, Chisso Corporation, 5-1 Ookawa, Kanazawa-Ku, Yokohama 236-8605, Japan.
authors.forename: Kazuya
authors.initials: K
authors.lastname: Yamanaka
authors.forename: Naoko
authors.initials: N
authors.lastname: Kito
authors.forename: Akihiro
authors.initials: A
authors.lastname: Kita
authors.forename: Yuuki
authors.initials: Y
authors.lastname: Imokawa
authors.forename: Chitose
authors.initials: C
authors.lastname: Maruyama
authors.forename: Takashi
authors.initials: T
authors.lastname: Utagawa
authors.forename: Yoshimitsu
authors.initials: Y
authors.lastname: Hamano
mesh_terms: D002384:Catalysis; D005285:Fermentation; D008565:Membrane Proteins / Q000378:metabolism; D016297:Mutagenesis, Site-Directed; D046908:Peptide Biosynthesis, Nucleic Acid-Independent; D010453:Peptide Synthases / Q000378:metabolism*; D011107:Polylysine / Q000096:biosynthesis*; D058105:Polymerization; D020539:Sequence Analysis, Protein; D013302:Streptomyces / Q000378:metabolism
chemical_list: D008565:Membrane Proteins; D011107:Polylysine; D010453:Peptide Synthases